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Bacterial biofilm extracellular matrix proteins are essential structural and functional elements of the extracellular polymeric substances (EPS) that surround and protect bacterial colonies. These proteins, including amyloid-like fibers such as Curli and TasA, as well as various adhesins and enzymes, provide the physical scaffold necessary for biofilm stability and surface attachment (Flemming & Wingender, 2010). In clinical settings, these proteins play a pivotal role in the pathogenesis of chronic infections by shielding bacteria from host immune cells and creating a barrier that impedes the penetration of antimicrobial agents (Karygianni et al., 2020). Therapeutic strategies targeting these protein substrates involve the use of exogenous proteases, such as serratiopeptidase or bromelain, to enzymatically degrade the matrix and promote biofilm dispersal (Selan et al., 2015). Additionally, monoclonal antibodies targeting highly conserved DNA-binding proteins (DNABII family) have shown efficacy in collapsing the biofilm architecture across multiple species (Goodman et al., 2011). By disrupting the proteinaceous framework, these therapies aim to restore antibiotic sensitivity and facilitate the clearance of persistent infections by the host immune system.
Enzymatic degradation of structural proteins, inhibition of amyloid fiber polymerization, and neutralization of DNA-binding proteins that stabilize the matrix scaffold to promote biofilm dispersal and antibiotic penetration.
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